Evidence for the Role of the monB Genes in Polyether Ring Formation during Monensin Biosynthesis

Chemistry and Biology

Volumn 13, Issue 4, 2006, Pages 453-460

  Gallimore, Andrew R ^a   Stark, Christian B W ^a   Bhatt, Apoorva ^a   Harvey, Barbara M ^a   Demydchuk, Yuliya ^a   Bolanos Garcia, Victor ^a   Fowler, Daniel J ^a   Staunton, James ^a   Leadlay, Peter F ^a   Spencer, Jonathan B ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

CHEMBIO; MICROBIO

Indexed keywords

BACTERIAL DNA; BACTERIAL PROTEIN; EPOXIDE HYDROLASE; LIMONENE 1,2 EPOXIDE HYDROLASE; LIMONENE-1,2-EPOXIDE HYDROLASE; MONENSIN;

AMINO ACID SEQUENCE; ARTICLE; BACTERIAL GENE; BIOSYNTHESIS; CHEMICAL STRUCTURE; CHEMISTRY; COMPARATIVE STUDY; ENZYMOLOGY; GENE DELETION; GENETICS; METABOLISM; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; RADIATION SCATTERING; RHODOCOCCUS; SEQUENCE HOMOLOGY; SPECIES DIFFERENCE; STREPTOMYCES;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BASE SEQUENCE; DNA, BACTERIAL; EPOXIDE HYDROLASES; GENE DELETION; GENES, BACTERIAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MONENSIN; RHODOCOCCUS; SCATTERING, RADIATION; SEQUENCE HOMOLOGY, AMINO ACID; SPECIES SPECIFICITY; STREPTOMYCES;

RHODOCOCCUS ERYTHROPOLIS;

EID: 33646059885     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2006.01.013     Document Type: Article

References (41)

1. Westley J.W. Polyethers. In: Corcoran J.W. (Ed). Antibiotics IV Biosynthesis (1981), Springer-Verlag Publishers, New York 41-73
2. Shimizu Y., Chou H.N., Bando H., Van Duyne G., and Clardy J. Structure of brevetoxin A (GB-1 toxin), the most potent toxin in the Florida red tide organism Gymnodinium breve (Ptychodiscus brevis). J. Am. Chem. Soc. 108 (1986) 514-515
3. Yasumoto T., and Murata M. Marine toxins. Chem. Rev. 93 (1993) 1897-1909
4. Riddell F.G. Ionophoric antibiotics. Chem. Br. 28 (1992) 533-537
5. 14C labelled substrates into lasalocid A. J. Antibiot. (Tokyo) 27 (1974) 288-297
6. Cane D.E., Liang T.-C., and Hasler H. Polyether biosynthesis. Origin of the oxygen atoms of monensin A. J. Am. Chem. Soc. 103 (1981) 5962-5965
7. Townsend C.A., and Basak A. Experiments and speculations on the role of oxidative cyclization chemistry in natural product biosynthesis. Tetrahedron 47 (1991) 2591-2602
8. Leadlay P.F., Staunton J., Oliynyk M., Bisang C., Cortés J., Frost E., Hughes-Thomas Z.A., Jones M.A., Kendrew S.G., Lester J.B., et al. Engineering of complex polyketide biosynthesis-insights from sequencing of the monensin biosynthetic gene cluster. J. Ind. Microbiol. Biotechnol. 27 (2001) 360-367
9. Oliynyk M., Stark C.B.W., Bhatt A., Jones M.A., Hughes-Thomas Z.A., Wilkinson C., Oliynyk Z., Demydchuk Y., Staunton J., and Leadlay P.F. Analysis of the biosynthetic gene cluster for the polyether antibiotic monensin in Streptomyces cinnamonensis and evidence for the role of monB and monC genes in oxidative cyclisation. Mol. Microbiol. 49 (2003) 1179-1190
10. Sun Y., Zhou X., Dong H., Tu G., Wang M., Wang B., and Deng Z. A complete gene cluster from Streptomyces nanchangensis NS3226 encoding biosynthesis of the polyether ionophore nanchangmycin. Chem. Biol. 10 (2003) 431-441
11. 5-3-ketosteroid isomerase from Pseudomonas testeroni. Biochemistry 37 (1998) 8325-8330
12. Bhatt A., Stark C.B.W., Harvey B.M., Gallimore A.R., Spencer J.B., Staunton J., and Leadlay P.F. Accumulation of an E,E,E,-triene by a polyether-producing polyketide synthase when oxidative cyclization is blocked. Angew. Chem. Int. Ed. Engl. 44 (2005) 7075-7078
13. Harvey B.M., Jones M.A., Hughes-Thomas Z.A., Goss R.M., Heathcote M.L., Bolanos-Garcia V.M., Kroutil W., Staunton J., Leadlay P.F., and Spencer J.B. Evidence that a novel thioesterase is responsible for polyketide chain release during biosynthesis of the polyether ionophore monensin. Chem. BiolChem. (2005) in press
14. Shi J., Blundell T.L., and Mizuguchi K. FUGUE: sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties. J. Mol. Biol. 310 (2001) 243-257
15. Lundqvist T., Rice J., Hodge C.N., Basarab G.S., Pierce J., and Lindqvist Y. Crystal structure of scytalone dehydratase-a disease determinant of the rice pathogen Magnaporthe grisea. Structure 2 (1994) 937-944
16. Arand M., Hallberg B.M., Zou J., Bergfors T., Oesch F., van der Werf J., de Bont J.A.M., Jones T.A., and Mowbray S.L. Structure of Rhodococcus erythropolis limonene-1,2-epoxide hydrolase reveals a novel active site. EMBO J. 22 (2003) 2583-2592
17. Sultana A., Kallio P., Jansson A., Wang J.S., Niemi J., Mantsala P., and Schneider G. Structure of the polyketide cyclase SnoaL reveals a novel mechanism for enzymatic aldol condensation. EMBO J. 23 (2004) 1911-1921
18. 5-3-ketosteroid isomerase with and without a reaction intermediate analogue. Biochemistry 36 (1997) 14030-14036
19. Holm L., and Sander C. Touring protein fold space with Dali/FSSP. Nucleic Acids Res. 26 (1998) 316-319
20. Robinson A., Wu P.S.-C., Harrop S.J., Schaeffer P.M., Dosztanyi Z., Gillings M.R., Holmes A.J., Nevalainen K.M.H., Stokes H.W., Otting G., et al. Integron-associated mobile gene cassettes code for folded proteins: the structure of Bal32a, a new member of the adaptable α + β barrel family. J. Mol. Biol. 346 (2005) 1229-1241
21. 2+/calmodulin-dependent kinase II. Mol. Cell 11 (2003) 1241-1251
22. Trewella J. Insights into biomolecular function from small-angle scattering. Curr. Opin. Struct. Biol. 7 (1997) 702-708
23. Lopes N.P., Stark C.B.W., Hong H., Gates P.J., and Staunton J. Fragmentation studies on monensin A and B by accurate mass electrospray tandem mass spectrometry. Rapid Commun. Mass. Spectrom. 16 (2002) 414-420
24. Perron F., and Albizati K.F. Chemistry of spiroketals. Chem. Rev. 89 (1989) 1617-1661
25. Ishihara J., Sugimoto T., and Murai A. Studies on the stability of 1,7,9-trioxadispiro[5.1.5.2]pentadecane system: the common tricyclic moiety in pinnatoxins. Synlett 6 (1998) 603-606
26. Baldwin J.E. Rules for ring closure. J. Chem. Soc. Chem. Comm. 11 (1976) 734-736
27. Hoye T.R., and Suhadolnik J.C. Symmetry-assisted synthesis of triepoxide stereoisomers of E,Z,E,-dodeca-2,6,10-trien-1,12-diol and their cascade reactions to 2,5-linked bistetrahydrofurans. J. Am. Chem. Soc. 107 (1985) 5312-5313
28. Koert U. Stereoselective synthesis of oligo-tetrahydrofurans. Synthesis (Mass.) 1995 (1995) 115-132
29. Arand M., Cronin A., Oesch F., Mowbray S.L., and Jones T.A. The tell-tale structures of epoxide hydrolases. Drug Metab. Rev. 35 (2003) 365-383
30. Jong R.M., and Dijkstra B.W. Structure and mechanism of bacterial dehalogenases: different ways to cleave a carbon-halogen bond. Curr. Opin. Struct. Biol. 13 (2003) 722-730
31. Rein K.S., and Borrone J. Polyketides from dinoflagellates: origins, pharmacology and biosynthesis. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 124 (1999) 117-131
32. Lee M.S., Qin G., Nakanishi K., and Zagorski M.G. Biosynthetic studies of brevetoxins, potent neurotoxins produced by the dinoflagellate Gymnodinium breve. J. Am. Chem. Soc. 111 (1989) 6234-6241
33. Semenyuk A.V., and Svergun D.I. GNOM - a program package for small-angle scattering data processing. J. Appl. Crystallogr. 24 (1991) 537-540
34. Svergun D.I., Petoukhov M.V., and Koch M.H.J. Determination of domain structure of proteins from X-ray solution scattering. Biophys. J. 80 (2001) 2946-2953
35. Altschul S.F., Madden T.L., Schaeffer A.A., Zhang J., Zhang Z., Miller W., and Lipman D.J. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 25 (1997) 3389-3402
36. De Bakker P.I.W., Bateman A., Burke D.F., Miguel R.N., Mizuguchi K., Shi J., and Blundell T.L. HOMSTRAD: adding sequence information to structure-based alignments of homologous protein families. Bioinformatics 17 (2001) 748-749
37. Mizuguchi K., Deane C.M., Blundell T.L., Johnson M.S., and Overington J.P. JOY: protein sequence-structure representation and analysis. Bioinformatics 14 (1998) 617-623
38. Sali A., and Blundell T.L. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234 (1993) 779-815
39. Laskowski R.A., MacArthur M.W., Moss D.S., and Thornton J.M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26 (1993) 283-291
40. Luthy R., Bowie J.U., and Eisenberg D. Assessment of protein models with three-dimensional profiles. Nature 356 (1992) 83-85
41. DeLano W.L. The PyMOL User's Manual (2002), DeLano Scientific, San Carlos, CA